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Ex.: O00571, ddx3x (keyword), ATP-dependent RNA helicase DDX3X, PXD000680 or 3JRV

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PDB 
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Phospho-sites

Showing 5 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
4 PhosphoS PRIDE yes
38 PhosphoS PRIDE yes
320 PhosphoT PRIDE yes
351 PhosphoS UP Combined
467 PhosphoS PRIDE yes

3D structure is not available

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Phosphorylated amino acids are colored red on the inner ring.

The first amino acid of the protein sequence is colored darker on each ring.

Phospho peptides

Showing 4 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
4 2 24 3 6
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 7 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD004415 5 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
PXD003531 32 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD002286 5 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD002394 2 Proteomic and phosphoproteomic analysis of cisplatin resistance in patient derived serous ovarian cancer Homo sapiens (Human) PARTIAL 2017-05-02 cell suspension culture
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
38 34 41 5 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 1 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
320 319 326 2 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004452 1 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD000680 1 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell
467 465 471 3 7
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000836 2 HOPE-fixation of lung tissue allows retrospective proteome and phosphoproteome studies Homo sapiens (Human) PARTIAL 2014-05-22 lung -
PXD000612 14 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD003531 37 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD002286 10 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 - -
PXD002394 1 Proteomic and phosphoproteomic analysis of cisplatin resistance in patient derived serous ovarian cancer Homo sapiens (Human) PARTIAL 2017-05-02 cell suspension culture -
PXD004452 2 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD001374 3 Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling Homo sapiens (Human) PARTIAL 2015-08-24 HeLa cell -

Structures

Showing 13 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5UJJ A X-ray 2.0999999046325684 2 B 0.44992447 38, 320, 351, 467
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 SER C 0.7 124.96508026123047 0.0
38 38 SER H 0.77 74.48869323730469 0.0
240 240 TYR H 1.0 11.461837768554688 0.0
320 320 THR H 1.0 0.16759192943572998 0.0
351 351 SER C 1.0 20.43506622314453 0.0
467 467 SER C 0.65 71.90445709228516 0.0
1R6U A X-ray 2.0 2 B 0.7571811 320, 351, 467
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
240 240 TYR H 1.0 3.6877872943878174 0.0
320 320 THR H 1.0 0.33458107709884644 0.0
351 351 SER C 1.0 19.51239013671875 0.0
467 467 SER C 0.65 59.74873352050781 0.0
1R6T A X-ray 2.0999999046325684 2 B 0.7733397 38, 320, 351
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
8 8 SER H 0.7 84.55109405517578 0.0
38 38 SER H 0.77 69.78016662597656 0.0
240 240 TYR H 1.0 3.9302265644073486 0.0
320 320 THR H 1.0 0.0 0.0
351 351 SER C 1.0 19.590103149414062 0.0
2QUI A X-ray 2.4000000953674316 2 B 0.55895996 320, 351, 467
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
240 240 TYR H 1.0 2.627235174179077 0.0
320 320 THR H 1.0 0.16348005831241608 0.0
351 351 SER C 1.0 24.256160736083984 0.0
467 467 SER C 0.65 82.98961639404297 0.0
2QUH A X-ray 2.4000000953674316 2 B 1.0 320, 351, 467
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
240 240 TYR H 1.0 3.5889928340911865 0.0
320 320 THR H 1.0 0.0 0.0
351 351 SER C 1.0 40.451194763183594 0.0
467 467 SER C 0.65 74.0980224609375 0.0
2QUJ A X-ray 2.4200000762939453 2 B 0.2776753 320, 351, 467
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
240 240 TYR H 1.0 2.5936479568481445 0.0
320 320 THR H 1.0 0.0 0.0
351 351 SER C 1.0 35.41352081298828 0.0
467 467 SER C 0.65 73.76245880126953 0.0
1O5T A X-ray 2.5 2 A 1.0 320, 351, 467
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
240 240 TYR H 1.0 4.189578533172607 0.0
320 320 THR H 1.0 6.361234664916992 0.0
351 351 SER C 1.0 47.195682525634766 0.0
467 467 SER C 0.65 74.50203704833984 0.0
2AZX A X-ray 2.799999952316284 4 [SO4]A:702 0.22732441 320, 351, 467
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
240 240 TYR H 1.0 3.404057025909424 0.0
320 320 THR H 1.0 0.33525940775871277 0.0
351 351 SER C 1.0 20.583528518676758 10.217489242553711
467 467 SER C 0.65 47.162532806396484 0.0
2QUK A X-ray 2.799999952316284 2 A 1.0 320, 351, 467
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
240 240 TYR H 1.0 2.2599544525146484 0.0
320 320 THR H 1.0 6.50002908706665 0.0
351 351 SER C 1.0 43.59367752075195 0.0
467 467 SER C 0.65 54.97215270996094 0.0
2DR2 A X-ray 3.0 4 [SO4]A:478 0.5230164 320, 351, 467
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
240 240 TYR H 1.0 2.300973415374756 0.0
320 320 THR H 1.0 0.0 0.0
351 351 SER C 1.0 43.399147033691406 9.16231632232666
467 467 SER C 0.65 78.3965835571289 0.0
2AKE A X-ray 3.0999999046325684 4 [SO4]A:478 0.5164243 320, 351, 467
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
240 240 TYR H 1.0 2.0924172401428223 0.0
320 320 THR H 1.0 0.0 0.0
351 351 SER C 1.0 46.91140365600586 5.842809677124023
467 467 SER C 0.65 72.3829116821289 0.0
5UJI A X-ray 2.7899999618530273 2 B 1.0 320, 467
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
240 240 TYR H 1.0 8.319067001342773 0.0
320 320 THR H 1.0 4.874179840087891 0.0
467 467 SER C 0.65 58.4952278137207 0.0
1ULH A X-ray 2.309999942779541 2 B 1.0
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
240 193 TYR H 1.0 3.4861831665039062 0.0
320 273 THR H 1.0 6.723264217376709 0.0
467 420 SER C 0.65 72.386962890625 0.0

Mutations

Showing 4 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
54 A S Polymorphism
257 H R Disease Neuronopathy, distal hereditary motor, 9 (HMN9) [MIM:617721]
443 A S Polymorphism
455 E D Unclassified A breast cancer sample